메뉴 건너뛰기




Volumn 42, Issue 8, 2014, Pages 5217-5233

The activation of the decapping enzyme DCP2 by DCP1 occurs on the EDC4 scaffold and involves a conserved loop in DCP1

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; ASPARAGINE; DCP1 PROTEIN; DCP2 PROTEIN; EDC4 PROTEIN; EXORIBONUCLEASE; NUCLEIC ACID BINDING PROTEIN; REGULATOR PROTEIN; UNCLASSIFIED DRUG; XRN1 PROTEIN;

EID: 84899794717     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gku129     Document Type: Article
Times cited : (86)

References (39)
  • 1
    • 84877792802 scopus 로고    scopus 로고
    • Structural and functional control of the eukaryotic mRNA decapping machinery
    • Arribas-Layton, M., Wu, D., Lykke-Andersen, J. and Song, H. (2013) Structural and functional control of the eukaryotic mRNA decapping machinery. Biochim. Biophys. Acta, 1829, 580-589.
    • (2013) Biochim. Biophys. Acta , vol.1829 , pp. 580-589
    • Arribas-Layton, M.1    Wu, D.2    Lykke-Andersen, J.3    Song, H.4
  • 2
    • 80053910875 scopus 로고    scopus 로고
    • Structural and functional insights into eukaryotic mRNA decapping
    • Ling, S.H., Qamra, R. and Song, H. (2011) Structural and functional insights into eukaryotic mRNA decapping. Wiley Interdiscip Rev. RNA, 2, 193-208.
    • (2011) Wiley Interdiscip Rev. RNA , vol.2 , pp. 193-208
    • Ling, S.H.1    Qamra, R.2    Song, H.3
  • 3
    • 84890703972 scopus 로고    scopus 로고
    • The role of disordered protein regions in the assembly of decapping complexes and RNP granules
    • Jonas, S. and Izaurralde, E. (2013) The role of disordered protein regions in the assembly of decapping complexes and RNP granules. Genes Dev., 27, 2628-2641.
    • (2013) Genes Dev. , vol.27 , pp. 2628-2641
    • Jonas, S.1    Izaurralde, E.2
  • 4
    • 0036888905 scopus 로고    scopus 로고
    • Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay
    • Lykke-Andersen, J. (2002) Identification of a human decapping complex associated with hUpf proteins in nonsense-mediated decay. Mol. Cell. Biol., 22, 8114-8121.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 8114-8121
    • Lykke-Andersen, J.1
  • 5
    • 0037121926 scopus 로고    scopus 로고
    • Human Dcp2: A catalytically active mRNA decapping enzyme located in specific cytoplasmic structures
    • van Dijk, E., Cougot, N., Meyer, S., Babajko, S., Wahle, E. and Seraphin, B. (2002) Human Dcp2: a catalytically active mRNA decapping enzyme located in specific cytoplasmic structures. EMBO J., 21, 6915-6924.
    • (2002) EMBO J. , vol.21 , pp. 6915-6924
    • Van Dijk, E.1    Cougot, N.2    Meyer, S.3    Babajko, S.4    Wahle, E.5    Seraphin, B.6
  • 8
    • 0033214061 scopus 로고    scopus 로고
    • The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif
    • Dunckley, T. and Parker, R. (1999) The DCP2 protein is required for mRNA decapping in Saccharomyces cerevisiae and contains a functional MutT motif. EMBO J., 18, 5411-5422.
    • (1999) EMBO J. , vol.18 , pp. 5411-5422
    • Dunckley, T.1    Parker, R.2
  • 9
    • 30044439885 scopus 로고    scopus 로고
    • Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe
    • She, M., Decker, C.J., Chen, N., Tumati, S., Parker, R. and Song, H. (2006) Crystal structure and functional analysis of Dcp2p from Schizosaccharomyces pombe. Nat. Struct. Mol. Biol., 13, 63-70.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 63-70
    • She, M.1    Decker, C.J.2    Chen, N.3    Tumati, S.4    Parker, R.5    Song, H.6
  • 11
    • 14944354785 scopus 로고    scopus 로고
    • Decapping reaction of mRNA requires Dcp1 in fission yeast: Its characterization in different species from yeast to human
    • Sakuno, T., Araki, Y., Ohya, Y., Kofuji, S., Takahashi, S., Hoshino, S. and Katada, T. (2004) Decapping reaction of mRNA requires Dcp1 in fission yeast: its characterization in different species from yeast to human. J. Biochem., 136, 805-812.
    • (2004) J. Biochem. , vol.136 , pp. 805-812
    • Sakuno, T.1    Araki, Y.2    Ohya, Y.3    Kofuji, S.4    Takahashi, S.5    Hoshino, S.6    Katada, T.7
  • 13
  • 14
    • 84857433862 scopus 로고    scopus 로고
    • Interdomain dynamics and coactivation of the mRNA decapping enzyme Dcp2 are mediated by a gatekeeper tryptophan
    • Floor, S.N., Borja, M.S. and Gross, J.D. (2012) Interdomain dynamics and coactivation of the mRNA decapping enzyme Dcp2 are mediated by a gatekeeper tryptophan. Proc. Natl Acad. Sci. USA, 109, 2872-2877.
    • (2012) Proc. Natl Acad. Sci. USA , vol.109 , pp. 2872-2877
    • Floor, S.N.1    Borja, M.S.2    Gross, J.D.3
  • 15
    • 29144481702 scopus 로고    scopus 로고
    • Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping
    • Fenger-Grøn, M., Fillman, C., Norrild, B. and Lykke-Andersen, J. (2005) Multiple processing body factors and the ARE binding protein TTP activate mRNA decapping. Mol. Cell, 20, 905-915.
    • (2005) Mol. Cell , vol.20 , pp. 905-915
    • Fenger-Grøn, M.1    Fillman, C.2    Norrild, B.3    Lykke-Andersen, J.4
  • 17
    • 79960838430 scopus 로고    scopus 로고
    • Identification and characterization of protein interactions in the mammalian mRNA processing body using a novel two-hybrid assay
    • Bloch, D.B., Nobre, R.A., Bernstein, G.A. and Yang, W.H. (2011) Identification and characterization of protein interactions in the mammalian mRNA processing body using a novel two-hybrid assay. Exp. Cell Res., 317, 2183-2199.
    • (2011) Exp. Cell Res. , vol.317 , pp. 2183-2199
    • Bloch, D.B.1    Nobre, R.A.2    Bernstein, G.A.3    Yang, W.H.4
  • 18
    • 0027320701 scopus 로고
    • A turnover pathway for both stable and unstable mRNAs in yeast: Evidence for a requirement for deadenylation
    • Decker, C.J. and Parker, R. (1993) A turnover pathway for both stable and unstable mRNAs in yeast: evidence for a requirement for deadenylation. Genes Dev., 7, 1632-1643.
    • (1993) Genes Dev. , vol.7 , pp. 1632-1643
    • Decker, C.J.1    Parker, R.2
  • 19
    • 0027214097 scopus 로고
    • Yeast cells lacking 5′!3′ exoribonuclease 1 contain mRNA species that are poly(A) deficient and partially lack the 5′ cap structure
    • Hsu, C.L. and Stevens, A. (1993) Yeast cells lacking 5′!3′ exoribonuclease 1 contain mRNA species that are poly(A) deficient and partially lack the 5′ cap structure. Mol. Cell. Biol., 13, 4826-4835.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4826-4835
    • Hsu, C.L.1    Stevens, A.2
  • 20
    • 0028202495 scopus 로고
    • Deadenylation of the unstable mRNA encoded by the yeast MFA2 gene leads to decapping followed by 5′!3′ digestion of the transcript
    • Muhlrad, D., Decker, C.J. and Parker, R. (1994) Deadenylation of the unstable mRNA encoded by the yeast MFA2 gene leads to decapping followed by 5′!3′ digestion of the transcript. Genes Dev., 8, 855-866.
    • (1994) Genes Dev. , vol.8 , pp. 855-866
    • Muhlrad, D.1    Decker, C.J.2    Parker, R.3
  • 21
    • 79952362044 scopus 로고    scopus 로고
    • Structural and biochemical studies of the 5′!3′ exoribonuclease Xrn1
    • Chang, J.H., Xiang, S., Xiang, K., Manley, J.L. and Tong, L. (2011) Structural and biochemical studies of the 5′!3′ exoribonuclease Xrn1. Nat. Struct. Mol. Biol., 18, 270-276.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 270-276
    • Chang, J.H.1    Xiang, S.2    Xiang, K.3    Manley, J.L.4    Tong, L.5
  • 22
    • 79951969817 scopus 로고    scopus 로고
    • Coupled 5′ nucleotide recognition and processivity in Xrn1-mediated mRNA decay
    • Jinek, M., Coyle, S.M. and Doudna, J.A. (2011) Coupled 5′ nucleotide recognition and processivity in Xrn1-mediated mRNA decay. Mol. Cell, 41, 600-608.
    • (2011) Mol. Cell , vol.41 , pp. 600-608
    • Jinek, M.1    Coyle, S.M.2    Doudna, J.A.3
  • 24
    • 33947540895 scopus 로고    scopus 로고
    • Arabidopsis DCP2, DCP1, and VARICOSE Form a Decapping complex required for postembryonic development
    • Xu, J., Yang, J.Y., Niu, Q.W. and Chua, N.H. (2006) Arabidopsis DCP2, DCP1, and VARICOSE Form a Decapping complex required for postembryonic development. Plant Cell, 18, 3386-3398.
    • (2006) Plant Cell , vol.18 , pp. 3386-3398
    • Xu, J.1    Yang, J.Y.2    Niu, Q.W.3    Chua, N.H.4
  • 25
    • 52949146385 scopus 로고    scopus 로고
    • The C-terminal region of Ge-1 presents conserved structural features required for P-body localization
    • Jinek, M., Eulalio, A., Lingel, A., Helms, S., Conti, E. and Izaurralde, E. (2008) The C-terminal region of Ge-1 presents conserved structural features required for P-body localization. RNA, 14, 1991-1998.
    • (2008) RNA , vol.14 , pp. 1991-1998
    • Jinek, M.1    Eulalio, A.2    Lingel, A.3    Helms, S.4    Conti, E.5    Izaurralde, E.6
  • 26
    • 0034704201 scopus 로고    scopus 로고
    • Human Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codon
    • Lykke-Andersen, J., Shu, M.D. and Steitz, J.A. (2000) Human Upf proteins target an mRNA for nonsense-mediated decay when bound downstream of a termination codon. Cell, 103, 1121-1131.
    • (2000) Cell , vol.103 , pp. 1121-1131
    • Lykke-Andersen, J.1    Shu, M.D.2    Steitz, J.A.3
  • 27
    • 84885356907 scopus 로고    scopus 로고
    • The SMG5-SMG7 heterodimer directly recruits the CCR4-NOT deadenylase complex to mRNAs containing nonsense codons via interaction with POP2
    • Loh, B., Jonas, S. and Izaurralde, E. (2013) The SMG5-SMG7 heterodimer directly recruits the CCR4-NOT deadenylase complex to mRNAs containing nonsense codons via interaction with POP2. Genes Dev., 27, 2125-2138.
    • (2013) Genes Dev. , vol.27 , pp. 2125-2138
    • Loh, B.1    Jonas, S.2    Izaurralde, E.3
  • 28
    • 79959992840 scopus 로고    scopus 로고
    • Deciphering correct strategies for multiprotein complex assembly by co-expression: Application to complexes as large as the histone octamer
    • Diebold, M.L., Fribourg, S., Koch, M., Metzger, T. and Romier, C. (2011) Deciphering correct strategies for multiprotein complex assembly by co-expression: application to complexes as large as the histone octamer. J. Struct. Biol., 175, 178-188.
    • (2011) J. Struct. Biol. , vol.175 , pp. 178-188
    • Diebold, M.L.1    Fribourg, S.2    Koch, M.3    Metzger, T.4    Romier, C.5
  • 29
    • 63849246525 scopus 로고    scopus 로고
    • Protein structure prediction on the web: A case study using the Phyre server
    • Kelley, L.A. and Sternberg, M.J.E. (2009) Protein structure prediction on the web: a case study using the Phyre server. Nat. Protocols, 4, 363-371.
    • (2009) Nat. Protocols , vol.4 , pp. 363-371
    • Kelley, L.A.1    Sternberg, M.J.E.2
  • 30
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high-density shaking cultures
    • Studier, W.F. (2005) Protein production by auto-induction in high-density shaking cultures. Prot. Exp. Pur., 1, 207-234.
    • (2005) Prot. Exp. Pur. , vol.1 , pp. 207-234
    • Studier, W.F.1
  • 31
    • 84870553285 scopus 로고    scopus 로고
    • Structural basis of the PNRC2-mediated link between mRNA surveillance and decapping
    • Lai, T., Cho, H., Liu, Z., Bowler, M.W., Piao, S., Parker, R., Kim, Y.K. and Song, H. (2012) Structural basis of the PNRC2-mediated link between mRNA surveillance and decapping. Structure, 20, 2025-2037.
    • (2012) Structure , vol.20 , pp. 2025-2037
    • Lai, T.1    Cho, H.2    Liu, Z.3    Bowler, M.W.4    Piao, S.5    Parker, R.6    Kim, Y.K.7    Song, H.8
  • 32
    • 28344456221 scopus 로고    scopus 로고
    • Ge-1 is a central component of the mammalian cytoplasmic mRNA processing body
    • Yu, J.H., Yang, W.H., Gulick, T., Bloch, K.D. and Bloch, D.B. (2005) Ge-1 is a central component of the mammalian cytoplasmic mRNA processing body. RNA, 11, 1795-1802.
    • (2005) RNA , vol.11 , pp. 1795-1802
    • Yu, J.H.1    Yang, W.H.2    Gulick, T.3    Bloch, K.D.4    Bloch, D.B.5
  • 33
    • 84883488802 scopus 로고    scopus 로고
    • Active site conformational dynamics are coupled to catalysis in the mRNA decapping enzyme dcp2
    • Aglietti, R.A., Floor, S.N., McClendon, C.L., Jacobson, M.P. and Gross, J.D. (2013) Active site conformational dynamics are coupled to catalysis in the mRNA decapping enzyme dcp2. Structure, 21, 1571-1580.
    • (2013) Structure , vol.21 , pp. 1571-1580
    • Aglietti, R.A.1    Floor, S.N.2    McClendon, C.L.3    Jacobson, M.P.4    Gross, J.D.5
  • 34
    • 8844245615 scopus 로고    scopus 로고
    • SMG7 acts as a molecular link between mRNA surveillance and mRNA decay
    • Unterholzner, L. and Izaurralde, E. (2004) SMG7 acts as a molecular link between mRNA surveillance and mRNA decay. Mol. Cell, 16, 587-596.
    • (2004) Mol. Cell , vol.16 , pp. 587-596
    • Unterholzner, L.1    Izaurralde, E.2
  • 35
    • 80053580757 scopus 로고    scopus 로고
    • GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets
    • Braun, J.E., Huntzinger, E., Fauser, M. and Izaurralde, E. (2011) GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets. Mol. Cell, 44, 120-133.
    • (2011) Mol. Cell , vol.44 , pp. 120-133
    • Braun, J.E.1    Huntzinger, E.2    Fauser, M.3    Izaurralde, E.4
  • 36
    • 84861866572 scopus 로고    scopus 로고
    • The mechanics of miRNA-mediated gene silencing: A look under the hood of miRISC
    • Fabian, M.R. and Sonenberg, N. (2012) The mechanics of miRNA-mediated gene silencing: a look under the hood of miRISC. Nat. Struct. Mol. Biol., 19, 586-593.
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 586-593
    • Fabian, M.R.1    Sonenberg, N.2
  • 39
    • 0032940545 scopus 로고    scopus 로고
    • Analysis of Muations of the yeast mRNA decapping enzyme
    • Tharun, S. and Parker, R. (1999) Analysis of Muations of the yeast mRNA decapping enzyme. Genetics, 151, 1273-1285.
    • (1999) Genetics , vol.151 , pp. 1273-1285
    • Tharun, S.1    Parker, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.